Site-specific cleavage of DNA-RNA hybrids by zinc finger/FokI cleavage domain fusions

Gene. 1997 Dec 5;203(1):43-9. doi: 10.1016/s0378-1119(97)00489-7.


Zinc-finger proteins of the Cys2His2 type bind DNA-RNA hybrids with affinities comparable to those for DNA duplexes. Such zinc-finger proteins were converted into site-specific cleaving enzymes by fusing them to the FokI cleavage domain. The fusion proteins are active and under optimal conditions cleave DNA duplexes in a sequence-specific manner. These fusions also exhibit site-specific cleavage of the DNA strand within DNA-RNA hybrids albeit at a lower efficiency (approximately 50-fold) compared to the cleavage of the DNA duplexes. These engineered endonucleases represent the first of their kind in terms of their DNA-RNA cleavage properties, and they may have important biological applications.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Base Sequence
  • Binding Sites
  • DNA / metabolism*
  • Deoxyribonucleases, Type II Site-Specific / metabolism*
  • Molecular Sequence Data
  • Nucleic Acid Hybridization*
  • RNA / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Zinc Fingers*


  • Recombinant Fusion Proteins
  • RNA
  • DNA
  • endodeoxyribonuclease FokI
  • Deoxyribonucleases, Type II Site-Specific